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The protein interaction network of a taxis signal transduction system... » Isaúde
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BMC microbiology [electronic resource]
2012-11-22 02:07:17

The protein interaction network of a taxis signal transduction system in a Halophilic Archaeon

Descrição: Background:The taxis signaling system of the extreme halophilic archaeon Halobacterium (Hbt.) salinarumdiffers in several aspects from its model bacterial counterparts Escherichia coli and Bacillus subtilis.We studied the protein interactions in the Hbt. salinarum taxis signaling system to gain anunderstanding of its structure, to gain knowledge about its known components and to search for newmembers.Results:The interaction analysis revealed that the core signaling proteins are involved in different proteincomplexes and our data provide evidence for dynamic interchanges between them. Fifteen of theeighteen taxis receptors (halobacterial transducers, Htrs) can be assigned to four different groupsdepending on their interactions with the core signaling proteins. Only one of these groups, whichcontains six of the eight Htrs with known signals, shows the composition expected for signalingcomplexes (receptor, kinase CheA, adaptor CheW, response regulator CheY). From the twoHbt. salinarum CheW proteins, only CheW1 is engaged in signaling complexes with Htrs and CheA,whereas CheW2 interacts with Htrs but not with CheA. CheY connects the core signaling structureto a subnetwork consisting of the two CheF proteins (which build a link to the flagellar apparatus),CheD (the hub of the subnetwork), two CheC complexes and the receptor methylesterase CheB.Conclusions:Based on our findings, we propose two hypotheses. First, Hbt. salinarum might have the capability todynamically adjust the impact of certain Htrs or Htr clusters depending on its current needs orenvironmental conditions. Secondly, we propose a hypothetical feedback loop from the responseregulator to Htr methylation made from the CheC proteins, CheD and CheB, which might contributeto adaptation analogous to the CheC/CheD system of B. subtilis.

Identificador: doi:10.1186/1471-2180-12-272
Volume: 0
Página: 2 a

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